Histidine-Lacked Aβ(1–16) Peptides: pH-Dependent Conformational Changes in Metal Ion Binding

Habasescu, Laura; Jureschi, Monica; Petre, Brînduşa Alina; Mihai, Marcela; Gradinaru, Robert �Vasile; Murariu, Manuela; Drochioiu, Gabi

doi:10.1007/s10989-020-10048-0

Cited by 6 publications

(6 citation statements)

References 45 publications

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“…The amidated peptide, NH 2 -FESNF-CO-NH 2 ( Figure 1 ) was synthesized by solid-phase peptide synthesis (SPPS) based on Fmoc/tBu strategy as previously described [ 32 , 33 , 34 ]. Rink amide resin (50–90 mesh, 0.51 mmol g −1 ) was used as a solid support.…”

Section: Methodsmentioning

confidence: 99%

A Diphenylalanine Based Pentapeptide with Fibrillating Self-Assembling Properties

et al. 2023

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Peptides and their related compounds can self-assemble into diverse nanostructures of different shapes and sizes in response to various stimuli such as pH, temperature or ionic strength. Here we report the synthesis and characterization of a lysozyme derived pentapeptide and its ability to build well-defined fibrillar structures. Lysozyme FESNF peptide fragment was synthesized by solid phase peptide synthesis using the Fmoc/t-Bu strategy, purified by analytical high-performance liquid chromatography (HPLC) and its molecular weight was confirmed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI–MS). Spectroscopic features of this pentapeptide were investigated by UV-visible spectroscopy and fluorimetry showing the pattern of marginal phenylalanine residues within the peptide sequence. Self-assembling properties were determined using atomic force microscopy (AFM), aggregation index and thioflavin T assay (ThT). FESNF generating fibrillar structures observed by AFM and aggregation propensity were primarily influenced by pH conditions. Moreover, the experimental data were confirmed by molecular dynamics simulation studies. The obtained fibrils will be used next to explore their potential to act as support material for medical and cosmetic application.

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Section: Methodsmentioning

confidence: 99%

A Diphenylalanine Based Pentapeptide with Fibrillating Self-Assembling Properties

et al. 2023

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“…More detailed description of solid phase peptide synthesis was provided in our previous papers [ 30 , 32 ]. The sequence of Aβ (1–16) and those of the newly synthesised peptides were: Aβ (1–16) :H- 1 DAEFR H DSGYEV HH QK 16 -NH 2 , Aβ (1–16) A 3 6,13,14 : H- 1 DAEFR A DSGYEV AA QK 16 -NH 2 , and Aβ (1–16) S 3 6,13,14 :H- 1 DAEFR S DSGYEV SS QK 16 -NH 2 .…”

Section: Methodsmentioning

confidence: 99%

“…If a molecular ion of a metal complex is fragmented, the fragment containing the metal ion can be stabilised and coordination sites can be determined by collision-induced dissociation (CID). The structure of Aβ (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16) was also investigated by tandem mass spectrometry (MS/MS), based on a collision-induced dissociation process [32]. The most intense peak in the mass spectrum, belonging to the [M + 3H] 3+ ion, was selected and subjected to MS/MS fragmentation (Figure 1b).…”

Section: Peptide Synthesismentioning

confidence: 99%

“…More detailed description of solid phase peptide synthesis was provided in our previous papers [30,32]. The sequence of Aβ (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16) and those of the newly synthesised peptides were: Aβ (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)…”

Section: Synthesis Of Aβ Peptide Fragmentsmentioning

confidence: 99%

“…Experiments based on MS, infrared (IR), UV–vis and microscopic techniques revealed significant changes in the structure of peptides, including their aggregation and fibrillation, associated with metal binding [ 26 , 27 , 28 , 29 ]. We have recently been looking for evidence of such complexity using MS and other bioanalytical techniques [ 30 , 31 , 32 ].…”

Section: Introductionmentioning

confidence: 99%

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Aluminium Binding to Modified Amyloid-β Peptides: Implications for Alzheimer’s Disease

2020

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Aluminium (Al) is clearly neurotoxic and considerable evidence exists that Al may play a role in the aetiology or pathogenesis of Alzheimer’s disease (AD). Nevertheless, the link between AD pathology and Al is still open to debate. Therefore, we investigated here the interaction of aluminium ions with two Aβ peptide fragments and their analogues. First, we synthesised by the Fmoc/tBu solid-phase peptide synthesis (SPPS) strategy using an automated peptide synthesiser two new peptides starting from the Aβ(1–16) native peptide fragment. For this purpose, the three histidine residues (H6, H13, and H14) of the Aβ(1–16) peptide were replaced by three alanine and three serine residues to form the modified peptides Aβ(1–16)A36,13,14 and Aβ(1–16)S36,13,14 (primary structures: H-1DAEFRADSGYEVAAQK16-NH2 and H-1DAEFRSDSGYEVSSQK16-NH2). In addition, the Aβ(9–16) peptide fragment (H-9GYEVHHQK16-NH2) and its glycine analogues, namely Aβ(9–16)G110, (H-9GGEVHHQK16-NH2), Aβ(9–16)G213,14 (H-9GYEVGGQK16-NH2), and Aβ(9–16)G310,13,14 (H-9GGEVGGQK16-NH2), were manually synthesised in order to study Al binding to more specific amino acid residues. Both the peptides and the corresponding complexes with aluminium were comparatively investigated by mass spectrometry (MS), circular dichroism spectroscopy (CD), atomic force microscopy (AFM), scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FT-IR). Al–peptide molecular ions and Al-fragment ions were unambiguously identified in the MS and MS/MS spectra. AFM images showed dramatic changes in the film morphology of peptides upon Al binding. Our findings from the investigation of N-terminal 1-16 and even 9-16 normal and modified sequences of Aβ peptides suggest that they have the capability to be involved in aluminium ion binding associated with AD.

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Structural Characterization of a New Collagen Biomimetic Octapeptide with Nanoscale Self‐Assembly Potential: Experimental and Theoretical Approaches

et al. 2022

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Bioinspired peptides are attractive biomolecules which can improve our understanding of self-assembly processes for rational design of new peptide-based materials. Herein, a new amidated peptide FRSAPFIE (FRS), based on a sequence present in human collagen, was synthesized, characterized by mass spectrometry and subjected to self-assembling investigations. The optimal conditions for self-assembly were disclosed by dynamic light scattering at 32 °C and a peptide concentration of 0.51 %. In addition, AFM studies revealed ellipsoidal FRS shapes with an area between 0.8 and 3.1 μm 2 . The ability of selfassembly was also proved using FAD dye as extrinsic fluorescence reporter. According to the theoretical analysis, the FRS peptide tends to form a bundle-type association, with a type of fibrillary tangles particle. Altogether, our findings address new challenges regarding the FRS peptide which can be used in further self-assembly studies to design biocompatible drug-delivery platforms.

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Histidine-Lacked Aβ(1–16) Peptides: pH-Dependent Conformational Changes in Metal Ion Binding

Cited by 6 publications

References 45 publications

A Diphenylalanine Based Pentapeptide with Fibrillating Self-Assembling Properties

A Diphenylalanine Based Pentapeptide with Fibrillating Self-Assembling Properties

Aluminium Binding to Modified Amyloid-β Peptides: Implications for Alzheimer’s Disease

Structural Characterization of a New Collagen Biomimetic Octapeptide with Nanoscale Self‐Assembly Potential: Experimental and Theoretical Approaches

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